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Concise Publication Free access | 10.1172/JCI107125
Thorndike Memorial Laboratory, Harvard Medical Service, Boston City Hospital, Boston 02118
Harvard Medical School, Boston, Massachusetts 02115
Department of Medicine, Ohio State University, Columbus, Ohio 43210
Department of Human Genetics, University of Michigan School of Medicine, Ann Arbor, Michigan 48105
Find articles by Bunn, H. in: JCI | PubMed | Google Scholar
Thorndike Memorial Laboratory, Harvard Medical Service, Boston City Hospital, Boston 02118
Harvard Medical School, Boston, Massachusetts 02115
Department of Medicine, Ohio State University, Columbus, Ohio 43210
Department of Human Genetics, University of Michigan School of Medicine, Ann Arbor, Michigan 48105
Find articles by Meriwether, W. in: JCI | PubMed | Google Scholar
Thorndike Memorial Laboratory, Harvard Medical Service, Boston City Hospital, Boston 02118
Harvard Medical School, Boston, Massachusetts 02115
Department of Medicine, Ohio State University, Columbus, Ohio 43210
Department of Human Genetics, University of Michigan School of Medicine, Ann Arbor, Michigan 48105
Find articles by Balcerzak, S. in: JCI | PubMed | Google Scholar
Thorndike Memorial Laboratory, Harvard Medical Service, Boston City Hospital, Boston 02118
Harvard Medical School, Boston, Massachusetts 02115
Department of Medicine, Ohio State University, Columbus, Ohio 43210
Department of Human Genetics, University of Michigan School of Medicine, Ann Arbor, Michigan 48105
Find articles by Rucknagel, D. in: JCI | PubMed | Google Scholar
Published November 1, 1972 - More info
Oxygen equilibrium was determined on hemoglobin of individuals both heterozygous and homozygous for hemoglobin E. The whole blood oxyhemoglobin dissociation curve of AE blood was identical to that of normal AA blood. E hemoglobin, isolated by diethylaminoethyl Sephadex and carboxymethyl cellulose column chromatography, had oxygen affinity, heme-heme interaction, and Bohr effect identical to those of hemoglobin A prepared from the same column. Furthermore, the two hemoglobins had equal reactivity with 2,3-diphosphoglycerate. Phosphate-free hemolysates of blood from E and A homozygotes also had identical oxygen saturation curves. These results do not confirm earlier reports that hemoglobin E has an abnormally low oxygen affinity.
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